Q1.

(a) Induced fit and lock and key are two models used to explain the action of
enzymes.

(i) Describe the induced fit model of enzyme action.

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(2)

(ii) Describe one way that the lock and key model is different from the induced fit
model.

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(1)

(b) Folic acid is a substance required by bacteria for cell growth. Bacteria produce folic
acid by the following reaction.

The diagram shows the structure of a molecule of PABA. It also shows the structure
of a molecule of a drug called sulfanilamide, which can be used to treat bacterial
infections. Sulfanilamide prevents bacteria producing folic acid.

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 Use the diagram and your knowledge of enzymes to explain how sulphanilamide
prevents bacteria producing folic acid.

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(3)
(Total 6 marks)

Q2. Gangliosides are lipids found in the cell surface membranes of nerve cells.
Hexosaminidase is an enzyme present in blood that breaks down gangliosides. If
gangliosides are not broken down, they damage nerve cells.

(a) Hexosaminidase only breaks down gangliosides. It does not break down other
lipids.

Explain why this enzyme only breaks down gangliosides.

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(3)

(b) Hexosaminidase is found in the blood of healthy people. People with Tay Sachs
disease do not have this enzyme in their blood.

Doctors confirm Tay Sachs disease by using a blood test. The technician carrying
out the test adds a solution containing a high concentration of gangliosides to a
sample of blood from the person being tested. The technician then measures the
concentration of gangliosides in the persons blood at regular intervals.

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 (i) Complete the graph below by sketching a curve to show the results you would
expect for a person with Tay Sachs disease. Label this curve T.

(1)

(ii) Sketch a curve on the same graph to show the results you would expect for a
healthy person who does not have Tay Sachs disease. Label this curve H.
(1)

(c) Scientists are trying to find a way to give the missing enzyme to people with Tay
Sachs disease. Suggest why they cannot give the enzyme as a tablet that is
swallowed.

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(2)
(Total 7 marks)

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Q3. The graph shows the effect of substrate concentration on the rate of an enzyme-
controlled reaction.

(a) (i) Describe what the graph shows about the effect of substrate concentration on
the rate of this enzyme-controlled reaction.

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(2)

(ii) What limits the rate of this reaction between points A and B? Give the
evidence from the graph for this.

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(2)

(iii) Suggest a reason for the shape of the curve between points C and D.

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(1)

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 (b) Sketch a curve on the graph to show the rate of this reaction in the presence of a
competitive inhibitor.
(1)

(c) Methotrexate is a drug used in the treatment of cancer. It is a competitive inhibitor

and affects the enzyme folate reductase.

(i) Explain how the drug lowers the rate of reaction controlled by folate reductase.

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(2)

(ii) Methotrexate only affects the rate of the reaction controlled by folate
reductase.

Explain why this drug does not affect other enzymes.

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(1)
(Total 9 marks)

Q4. (a) The diagrams represent an enzyme, its substrate and two other molecules, A
and B.

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 The addition of a non-competitive inhibitor will prevent the formation of an enzyme-
substrate complex. Draw a labelled diagram based on relevant molecules selected
from the diagram above to explain how this occurs.

(2)

(b) A decrease in temperature decreases the kinetic energy of molecules in a solution.

Explain how a decrease in temperature decreases the rate of an enzyme-controlled
reaction.

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(2)

(c) Urea breaks hydrogen bonds. Explain how the addition of urea would affect the rate
of an enzyme-controlled reaction.

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(3)
(Total 7 marks)

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M1. (a) (i) Active site/enzyme not complementary;

Active site changes (shape)/is flexible;

(Change in enzyme allows) substrate to fit/E-S complex to form;

Active site becomes complementary/wraps around substrate
= 2 marks
For mark point 2. allow binding site but not enzyme
For mark point 2. can only have enzyme changes (shape) if
active site has been mentioned earlier
Final mark point must have context
Reject: active site on substrate for second marking point only
Accept: diagrams only if suitably labelled or annotated
2 max

(ii) Active site does not change (shape)/is fixed (shape)/is rigid/does
not wrap around substrate/(already) fits the substrate/is
complementary (before binding);
Assume that it refers to lock and key
1

(b) Similar structure/shape (to PABA)/both complementary;

Competes for/binds to active site/competitive inhibitor;

Less PABA binds/less E-S complexes;

OR

Specific reference to different structure/shape (to PABA)

using the diagram;

Binds to position other than active site/binds to allosteric

site/binds to inhibitor site/non-competitive inhibitor;

Changes the active site so substrate cannot bind/less PABA

binds/less E-S complexes;
Q Reject: same structure/shape
Note: competitive inhibitor binds to active site = 1 mark
(same mark point)
Assume that it refers to sulfanilamide
Accept: PABA/substrate cannot bind
Neutral: less product produced as in question stem
Neutral: different structure/shape to PABA
Reject: active site on substrate for second marking point only
3 max

Page 7
 [6]

M2. (a) Active site;

(Complementary/specific) structure/shape;
(Only) fits/binds to gangliosides;
Forms enzyme-substrate complexes;

OR

Active site;
(Complementary/specific) structure/shape;
(Does not) fit/bind with other lipids;
Does not form enzyme-substrate complexes;
Note: active site has a specific shape = 2 marks;
Reject: same shape
Second mark for either route can refer to the enzyme or the
substrate
Accept: converse of second mark point and (different)
structure/shape if referring to other lipids
3 max

(b) (i) No change/substrate remains high/horizontal line;

Curve should be labelled
If curve H correctly labelled then assume other is curve T
Reject: obvious rise or fall/rise then plateau
1

(ii) Curve decreases rapidly at first then more slowly;

Curve should be labelled
If curve T correctly labelled then assume other is curve H
Reject: falling at a slower rate initially
1

(c) (Enzymes are) proteins;

Digested/broken down/destroyed (by enzymes/acid);

OR

(Enzymes are) too large;

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 To cross cell membranes/be absorbed/enter the bloodstream;
Accept: denatured (by acid)
Neutral: digested by saliva
Reject: digested by amylase
Neutral: will not reach the bloodstream
2
[7]

M3. (a) (i) Increases then plateaus/constant/steady/rate does not change;

Neutral: peaks/reaches a maximum/stops increasing/no
effect instead of plateaus
Reject: rate decreases/reaction stops

Correct reference. to 27/28 units;

e.g. increases up to/plateaus at 27/28
2

(ii) Substrate concentration/amount of substrate;

As substrate concentration increases, rate increases/positive

correlation (between rate and substrate concentration);
2

(iii) All active sites occupied/saturated/enzyme limiting (rate of

reaction)/maximum number of E-S complexes;
Reject: enzymes used up
Reject: substrate limits rate of reaction
Neutral: substrate no longer limits the reaction
Neutral: reference to temperature
1

(b) Curve is lower and plateaus at a higher substrate concentration

(it must also start at zero);
Accept: curve lower and joins existing curve at final point
(with no plateau)
Reject: if curve plateaus before original
Reject: if curve plateaus lower than original
1

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 (c) (i) Methotrexate/drug is a similar shape/structure to substrate;
Q Reject: same structure/shape

Binds to/fits/is complementary to active site;

Q Reject: reacts with active site

Less substrate binds/less enzyme-substrate complexes formed;

Accept: substrate cannot bind/enzyme-substrate complex
not formed
2 max

(ii) Methotrexate/drug is only similar shape to specific substrate/

only fits this active site;
Assume that it refers to the drug

OR

Methotrexate/drug is a different shape to other substrates/will

not fit other active sites;
1
[9]

M4. (a) diagram showing molecule A fitting in inhibition site; distortion

of active site;
2

(b) molecules moving less/slower; reduces chance of collision

(between enzyme and substrate)/of enzyme-substrate
complexes being formed; (reject converse)
2

(c) these bonds hold/maintain tertiary/globular structure (of enzyme);

enzyme denatured/tertiary structures destroyed; (shape of) active site
distorted/changes;
substrate no longer fits/enzyme-substrate complex not formed;
3 max
[7]

Page 10
E1. (a) Most candidates gained one mark for the idea that a change in the shape of the
enzyme allows the substrate to fit. Surprisingly, it was usually only better candidates that referred to
the active site of the enzyme. Some weaker candidates placed the active site on the substrate.

Half of the candidates gained this mark for stating that the active site is a fixed
shape in the lock and key model or already complementary to the substrate. Weaker
candidates did not refer to the active site.

(b) Over half of the candidates gained at least two marks for noting that sulfanilamide
acts as a competitive inhibitor, which prevents PABA from binding. Many candidates
were also aware of the importance of shape. However, this mark was sometimes
disqualified for stating that sulfanilamide and PABA are the same shape. Weaker
candidates were let down by poor expression. They referred to inhibiting bacteria or
placed the active site on PABA or sulfanilamide. A minority of candidates focused on
folic acid and went on to describe enzyme denaturation by the acid. Few candidates
took the non-competitive inhibitor route of the mark scheme. However, those who
did often scored two marks.

E2. (a) Just over 60% of candidates scored full marks for this question. Many
candidates understood that the active site has a specific or complementary shape,
which ensures that only gangliosides can bind. Candidates who did not gain full
credit usually referred to the enzyme rather than the active site. A minority of weaker
candidates placed the active site on the substrate.

(b) Some candidates failed to score on parts (i) or (ii) through not reading the question
stem carefully. Consequently, curves were drawn without labels or that did not start
at the point required. A wide variety of curve shapes was seen for both question
parts.

(c) Approximately one fifth of candidates scored full marks for this question. This was
usually for taking the second route in the mark scheme and stating that enzymes are
Page 11
 too large to be absorbed. Most candidates who took the first route were aware that
enzymes could be digested if taken orally. However, relatively few recalled that
enzymes are proteins.

E3. (a) (i) Most candidates gained one mark for describing that the rate of reaction
increased and then remained constant. Unfortunately, a minority of candidates
disqualified this mark by stating that the plateau was where the reaction had
stopped or the rate had decreased. Surprisingly, very few candidates correctly
identified the substrate concentration at which the rate of reaction started to
level off. Many simply referred to point B on the graph, or typically gave a
value from 20-25. A minority of candidates gave an explanation for the shape
of the curve.

(ii) Most candidates were aware that substrate concentration was limiting the rate
of reaction. Many then went on to explain correctly how this could be
determined from the graph. A minority of candidates did not read the question
stem carefully and referred to the curve after point B. References to
temperature as the limiting factor were not credited as this could not be
determined from the graph.

(iii) This proved to be a good discriminator. Just less than half of candidates
gained this mark for explaining that all active sites were occupied or that
enzyme concentration was a limiting factor. Weaker candidates were often let
down by poor expression or a lack of detail e.g. enzymes working flat out, all
enzymes are active, enzymes are at saturation point and maximum number
of collisions. As was the case for (a)(i), a minority of candidates thought that
the reaction had stopped between points C and D. Other incorrect
explanations seen included reference to enzyme denaturation and the
presence of an inhibitor.

(b) Almost half of candidates scored one mark. Many candidates who failed to score
were aware that the initial rate of reaction would be lower. However, they usually
confused the two types of enzyme inhibitor and drew the plateau below that of the
original curve.

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 (c) (i) Most candidates gained at least one mark for stating that the drug would bind
to the active site. Weaker candidates sometimes missed out on this mark
through a lack of detail e.g. the drug binds to the enzyme. Better candidates
usually went on to score full marks for the idea that less enzyme-substrate
complexes would form. References to the drug having a similar shape to the
substrate were less frequent. However, some candidates disqualified this for
stating that the drug was the same shape as the substrate or active site.

(ii) Just less than half of candidates gained the mark for explaining that the drug
could only fit the active site of folate reductase. This was expressed in a
variety of ways but typically in terms of the complementary shapes of drug and
active site. Very few candidates gained the mark for explaining that the drug
was a similar shape to only one substrate. Weaker candidates often wrote in
general terms about enzyme specificity, without reference to the drug.
Similarly, as in (c)(i), poor expression prevented some candidates from
scoring. This was usually for referring to the enzyme rather than active site or
for stating that the drug was the same shape as the active site.

E4. (a) Revealed an excellent understanding of non-competitive inhibition and there

were many correct answers. Occasionally candidates involved both molecules A
and B or attempted to make up an entirely different molecule which they attached to
the side of the enzyme.

(b) Most answers indicated that fewer collisions resulted in fewer enzyme-substrate
complexes being formed, even if this was explained simply in terms of lower kinetic
energy, information provided in the question. It should be noted that answers based
on an increase in temperature were unacceptable as were those responses based
on denaturation.

(c) Although there were many excellent answers, less able candidates were often
unable to apply their knowledge to this unfamiliar example. The most common
incorrect responses were based on urea increasing the rate of reaction, either by
somehow assisting enzymes in breaking hydrogen bonds in the substrate or in
breaking the bonds binding substrates to active sites.

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